ID D9S0D1_THEOJ Unreviewed; 308 AA.
AC D9S0D1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Molybdenum cofactor synthesis domain protein {ECO:0000313|EMBL:ADL07059.1};
GN OrderedLocusNames=Toce_0276 {ECO:0000313|EMBL:ADL07059.1};
OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS JW/IW-1228P).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermosediminibacter.
OX NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL07059.1, ECO:0000313|Proteomes:UP000000272};
RN [1] {ECO:0000313|EMBL:ADL07059.1, ECO:0000313|Proteomes:UP000000272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC {ECO:0000313|Proteomes:UP000000272};
RX PubMed=21304740;
RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Thermosediminibacter oceani type strain
RT (JW/IW-1228P).";
RL Stand. Genomic Sci. 3:108-116(2010).
CC -!- FUNCTION: May be involved in the biosynthesis of molybdopterin.
CC {ECO:0000256|ARBA:ARBA00003487}.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
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DR EMBL; CP002131; ADL07059.1; -; Genomic_DNA.
DR RefSeq; WP_013275110.1; NC_014377.1.
DR AlphaFoldDB; D9S0D1; -.
DR STRING; 555079.Toce_0276; -.
DR KEGG; toc:Toce_0276; -.
DR eggNOG; COG0521; Bacteria.
DR eggNOG; COG2258; Bacteria.
DR HOGENOM; CLU_077358_3_0_9; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000000272; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR005302; MoCF_Sase_C.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR43764; MOLYBDENUM COFACTOR BIOSYNTHESIS; 1.
DR PANTHER; PTHR43764:SF1; MOLYBDOPTERIN MOLYBDOTRANSFERASE; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR Pfam; PF03473; MOSC; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS51340; MOSC; 1.
PE 4: Predicted;
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000000272}.
FT DOMAIN 18..142
FT /note="MOSC"
FT /evidence="ECO:0000259|PROSITE:PS51340"
SQ SEQUENCE 308 AA; 33206 MW; 03237ED93E5B0CBA CRC64;
MGKVVAVCVS EKKGEKKRDV GKAMLIEGFG IEGDAHAGAW HRQVSLLALE SIDKMREKGL
SVGPGDFAEN ITTEGIDLSS LPVGTRLRIN DVLLEVTQIG KECHERCAIY RQAGDCIMPK
EGIFARVLRG GVVSAGDEIE VIPVIRVGIL TASDRGAKGE REDLSGKVIE EMMEAVNGRI
EEYVMVPDDL EAIKNSLLAM CEKGLDLVLT TGGTGLSPRD NTPEATLAVV EKQVPGIPEA
MRQKSLEKTP NAMLSRAVAG IRGRTLIINL PGSPKAVREN LEVVLPALPH AVELLRGRVR
DCGRPDRH
//